User:Peter Chien: Difference between revisions

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==Research interests==
==Research interests==
<!-- Feel free to add brief descriptions to your research interests as well -->
<!-- Feel free to add brief descriptions to your research interests as well -->
# Interest 1
 
# Interest 2
Protein degradation is an essential process for all biological life.  Damaged or improperly folded proteins need to be cleared from the cell before they elicit toxic effects.  Regulatory proteins need to be degraded so that the response they support exists only as long as it is necessary.  However, as proteolysis is an irreversible event, great care must be taken to only degrade those factors as needed without disturbing the balance of other proteins.  In eukaryotes, exquisite selectivity is generated through cascading molecular events that together yield a ubiquitination signal which targets a substrate for degradation.  As no such system exists in bacteria, the highly specific nature of protein degradation must be accomplished at the level of direct recognition of the substrate or by utilizing auxiliary factors to improve specificity.  The general objectives of the Chien lab are to understand how these substrates are recognized in a precise fashion and the impact of substrate degradation on the various regulatory networks of the cell.
# Interest 3


==Publications==
==Publications==

Revision as of 19:21, 15 March 2010

Contact Info

Peter Chien (an artistic interpretation)

I work at UMass Amherst in the Biochemistry and Molecular Biology Department. I learned about OpenWetWare when I was at MIT for my postdoc, and, although initially scared off by Jason and Barry - I've joined because I like the sharing of information/resources/science.

Education

  • 2003-2009, postdoc, MIT
  • 2003, PhD Biophysics, UCSF
  • 1998, BS Physics/Biology, MIT

Research interests

Protein degradation is an essential process for all biological life. Damaged or improperly folded proteins need to be cleared from the cell before they elicit toxic effects. Regulatory proteins need to be degraded so that the response they support exists only as long as it is necessary. However, as proteolysis is an irreversible event, great care must be taken to only degrade those factors as needed without disturbing the balance of other proteins. In eukaryotes, exquisite selectivity is generated through cascading molecular events that together yield a ubiquitination signal which targets a substrate for degradation. As no such system exists in bacteria, the highly specific nature of protein degradation must be accomplished at the level of direct recognition of the substrate or by utilizing auxiliary factors to improve specificity. The general objectives of the Chien lab are to understand how these substrates are recognized in a precise fashion and the impact of substrate degradation on the various regulatory networks of the cell.

Publications

  1. Chowdhury T, Chien P, Ebrahim S, Sauer RT, and Baker TA. Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species. Protein Sci. 2010 Feb;19(2):242-54. DOI:10.1002/pro.306 | PubMed ID:20014030 | HubMed [Paper1]
  2. Kobayashi H, De Nisco NJ, Chien P, Simmons LA, and Walker GC. Sinorhizobium meliloti CpdR1 is critical for co-ordinating cell cycle progression and the symbiotic chronic infection. Mol Microbiol. 2009 Aug;73(4):586-600. DOI:10.1111/j.1365-2958.2009.06794.x | PubMed ID:19602145 | HubMed [Paper2]
  3. Chien P, Grant RA, Sauer RT, and Baker TA. Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors. Structure. 2007 Oct;15(10):1296-305. DOI:10.1016/j.str.2007.08.008 | PubMed ID:17937918 | HubMed [Paper3]
  4. Chien P, Perchuk BS, Laub MT, Sauer RT, and Baker TA. Direct and adaptor-mediated substrate recognition by an essential AAA+ protease. Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6590-5. DOI:10.1073/pnas.0701776104 | PubMed ID:17420450 | HubMed [Paper4]

    leave a comment about a paper here

All Medline abstracts: PubMed | HubMed

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